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Literature summary for 1.14.13.39 extracted from
- Subunit dissociation and unfolding of macrophage NO synthase: relationship between enzyme structure, prosthetic group binding, and catalytic function (1995), Biochemistry, 34, 11167-11175.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| dithiothreitol | - |
Mus musculus |  |
| interferon gamma | activates | Mus musculus | |
| lipopolysaccharide | from Escherichia coli, activates | Mus musculus | |
General Stability
| General Stability | Organism |
|---|---|
| bovine serum albumin stabilizes during refolding | Mus musculus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | protoporphyrin IX heme | Mus musculus | |
| Iron | 0.83 mol per mol of subunit | Mus musculus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 130000 | - |
2 * 130000, SDS-PAGE | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
cytokine-inducible in macrophage | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| dimeric enzyme and subunits | Mus musculus |
| from interferon-gamma- and lipopolysaccharide-activated macrophage | Mus musculus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | relation between structure, function and binding of prosthetic groups during dissociation, unfolding and renaturation | Mus musculus |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| refolding after treatment/equilibration with 5 M urea in presence of L-arginine and tetrahydrobiopterin | Mus musculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| macrophage | RAW 264.7 cells | Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 L-arginine + 3 NADPH + 4 O2 + 3 H+ | - |
Mus musculus | 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 130000, SDS-PAGE | Mus musculus |
| More | dimer formation, each subunit consists of: 1 oxygenase domain containing heme, tetrahydrobiopterin, substrate binding site and 1 reductase domain containing FAD, FMN, calmodulin, NADPH binding site | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| i-NOS | isoform II, inducible | Mus musculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mus musculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | - |
assay at | Mus musculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 5,6,7,8-tetrahydro-L-biopterin | 0.04 mol per mol of subunit | Mus musculus | |
| FAD | - |
Mus musculus | |
| FMN | - |
Mus musculus | |
| NADPH | - |
Mus musculus | |
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